ID   CBH_LACPL               Reviewed;         324 AA.
AC   Q06115; F9UUJ8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Conjugated bile acid hydrolase {ECO:0000303|PubMed:1476424};
DE            EC=3.5.1.- {ECO:0000269|PubMed:1476424};
DE   AltName: Full=Bile salt hydrolase;
DE            Short=BSH;
DE   AltName: Full=Choloylglycine hydrolase {ECO:0000303|PubMed:1476424};
DE            EC=3.5.1.24 {ECO:0000269|PubMed:1476424};
GN   Name=cbh {ECO:0000303|PubMed:1476424}; Synonyms=bsh;
GN   OrderedLocusNames=lp_3536;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=DSM 4229 / 80;
RX   PubMed=1476424; DOI=10.1128/aem.58.12.3792-3798.1992;
RA   Christiaens H., Leer R.J., Pouwels P.H., Verstraete W.;
RT   "Cloning and expression of a conjugated bile acid hydrolase gene from
RT   Lactobacillus plantarum by using a direct plate assay.";
RL   Appl. Environ. Microbiol. 58:3792-3798(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
CC   -!- FUNCTION: Bile salt hydrolase that catalyzes the deconjugation of
CC       glycine- and taurine-linked bile salts, which occurs naturally in the
CC       intestines of animals, releasing amino acid residues and deconjugated
CC       bile salts (bile acids). Can hydrolyze the amid bond in the bile salts
CC       glycocholate (GCA), glycodeoxycholate (GDCA), glycochenodeoxycholate
CC       (GCDCA), taurocholate (TCA), taurodeoxycholate (TDCA) and
CC       taurochenodeoxycholate (TCDCA). Shows a preference for glycine-
CC       conjugated bile acids as substrates. {ECO:0000269|PubMed:1476424}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycocholate + H2O = cholate + glycine; Xref=Rhea:RHEA:19353,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:29746, ChEBI:CHEBI:29747,
CC         ChEBI:CHEBI:57305; EC=3.5.1.24;
CC         Evidence={ECO:0000269|PubMed:1476424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19354;
CC         Evidence={ECO:0000305|PubMed:1476424};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycodeoxycholate + H2O = deoxycholate + glycine;
CC         Xref=Rhea:RHEA:47552, ChEBI:CHEBI:15377, ChEBI:CHEBI:23614,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:82982;
CC         Evidence={ECO:0000269|PubMed:1476424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47553;
CC         Evidence={ECO:0000305|PubMed:1476424};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chenodeoxycholate + glycine = glycochenodeoxycholate + H2O;
CC         Xref=Rhea:RHEA:47112, ChEBI:CHEBI:15377, ChEBI:CHEBI:36234,
CC         ChEBI:CHEBI:36252, ChEBI:CHEBI:57305;
CC         Evidence={ECO:0000269|PubMed:1476424};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:47114;
CC         Evidence={ECO:0000305|PubMed:1476424};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholate + taurine = H2O + taurocholate; Xref=Rhea:RHEA:47108,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:29747, ChEBI:CHEBI:36257,
CC         ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:1476424};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:47110;
CC         Evidence={ECO:0000305|PubMed:1476424};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + taurodeoxycholate = deoxycholate + taurine;
CC         Xref=Rhea:RHEA:47556, ChEBI:CHEBI:15377, ChEBI:CHEBI:23614,
CC         ChEBI:CHEBI:36261, ChEBI:CHEBI:507393;
CC         Evidence={ECO:0000269|PubMed:1476424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47557;
CC         Evidence={ECO:0000305|PubMed:1476424};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + taurochenodeoxycholate = chenodeoxycholate + taurine;
CC         Xref=Rhea:RHEA:16309, ChEBI:CHEBI:9407, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:36234, ChEBI:CHEBI:507393;
CC         Evidence={ECO:0000269|PubMed:1476424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16310;
CC         Evidence={ECO:0000305|PubMed:1476424};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.22 mM for glycodeoxycholate {ECO:0000269|PubMed:1476424};
CC         Vmax=1.56 umol/min/mg enzyme with glycodeoxycholate as substrate
CC         {ECO:0000269|PubMed:1476424};
CC       pH dependence:
CC         Optimum pH is 4.7-5.5. {ECO:0000269|PubMed:1476424};
CC       Temperature dependence:
CC         Optimum temperature is 30-45 degrees Celsius.
CC         {ECO:0000269|PubMed:1476424};
CC   -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC       {ECO:0000305|PubMed:1476424}.
CC   -!- SUBUNIT: Homotetramer. The tetramer consists of a dimer of dimers.
CC       {ECO:0000250|UniProtKB:P54965}.
CC   -!- SIMILARITY: Belongs to the peptidase C59 family. {ECO:0000305}.
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DR   EMBL; S51638; AAB24746.1; -; Genomic_DNA.
DR   EMBL; M96175; AAA25233.1; -; Genomic_DNA.
DR   EMBL; AL935263; CCC80500.1; -; Genomic_DNA.
DR   PIR; A48953; A48953.
DR   RefSeq; WP_011102211.1; NC_004567.2.
DR   RefSeq; YP_004891014.1; NC_004567.2.
DR   AlphaFoldDB; Q06115; -.
DR   SMR; Q06115; -.
DR   STRING; 220668.lp_3536; -.
DR   MEROPS; C59.951; -.
DR   EnsemblBacteria; CCC80500; CCC80500; lp_3536.
DR   GeneID; 77216564; -.
DR   KEGG; lpl:lp_3536; -.
DR   PATRIC; fig|220668.9.peg.2947; -.
DR   eggNOG; COG3049; Bacteria.
DR   HOGENOM; CLU_045206_1_1_9; -.
DR   OrthoDB; 9794717at2; -.
DR   PhylomeDB; Q06115; -.
DR   BRENDA; 3.5.1.24; 2849.
DR   UniPathway; UPA00221; -.
DR   Proteomes; UP000000432; Chromosome.
DR   GO; GO:0047742; F:chenodeoxycholoyltaurine hydrolase activity; IEA:RHEA.
DR   GO; GO:0045302; F:choloylglycine hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006699; P:bile acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00542; Ntn_PVA; 1.
DR   InterPro; IPR047711; CBAH.
DR   InterPro; IPR029132; CBAH/NAAA_C.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   NCBIfam; NF038245; bile_salt_hydro; 1.
DR   PANTHER; PTHR35527; CHOLOYLGLYCINE HYDROLASE; 1.
DR   PANTHER; PTHR35527:SF2; HYDROLASE-RELATED; 1.
DR   Pfam; PF02275; CBAH; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Lipid metabolism; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..324
FT                   /note="Conjugated bile acid hydrolase"
FT                   /id="PRO_0000073020"
FT   ACT_SITE        2
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P54965"
FT   BINDING         2
FT                   /ligand="deoxycholate"
FT                   /ligand_id="ChEBI:CHEBI:23614"
FT                   /evidence="ECO:0000250|UniProtKB:P54965"
FT   BINDING         16
FT                   /ligand="deoxycholate"
FT                   /ligand_id="ChEBI:CHEBI:23614"
FT                   /evidence="ECO:0000250|UniProtKB:P54965"
FT   BINDING         79
FT                   /ligand="taurine"
FT                   /ligand_id="ChEBI:CHEBI:507393"
FT                   /evidence="ECO:0000250|UniProtKB:P54965"
FT   CONFLICT        236
FT                   /note="S -> P (in Ref. 1; AAB24746/AAA25233)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="S -> N (in Ref. 1; AAB24746/AAA25233)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   324 AA;  37042 MW;  B5E53F74AD742347 CRC64;
     MCTAITYQSY NNYFGRNFDY EISYNEMVTI TPRKYPLVFR KVENLDHHYA IIGITADVES
     YPLYYDAMNE KGLCIAGLNF AGYADYKKYD ADKVNITPFE LIPWLLGQFS SVREVKKNIQ
     KLNLVNINFS EQLPLSPLHW LVADKQESIV IESVKEGLKI YDNPVGVLTN NPNFDYQLFN
     LNNYRALSNS TPQNSFSEKV DLDSYSRGMG GLGLPGDLSS MSRFVRAAFT KLNSLSMQTE
     SGSVSQFFHI LGSVEQQKGL CEVTDGKYEY TIYSSCCDMD KGVYYYRTYD NSQINSVSLN
     HEHLDTTELI SYPLRSEAQY YAVN
//